› 8p1g

X-ray diffraction
1.42Å resolution

Crystal structure of inactive TtCE16 in complex with acetate

Released:
DOI: 10.2210/pdb8p1g/pdb
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PDB entry 8p1g coloured by chain, front view.
PDB entry 8p1g coloured by chain, side view.
PDB entry 8p1g coloured by chain, top view.
Source organism: Thermothelomyces thermophilus
Primary publication:
The role of CE16 exo-deacetylases in hemicellulolytic enzyme mixtures revealed by the biochemical and structural study of the novel TtCE16B esterase.
Pentari C, Zerva A, Kosinas C, Karampa P, Puchart V, Dimarogona M, Topakas E
Carbohydr Polym 327 121667 (2024)
PMID: 38171682

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-227082 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (3 distinct):
Carbohydrate esterase family 16 protein Chain: B
Molecule details ›
Chain: B
Length: 353 amino acids
Theoretical weight: 39.49 KDa
Source organism: Thermothelomyces thermophilus
Expression system: Komagataella pastoris
UniProt:
  • Canonical: G2QL32 (Residues: 16-343; Coverage: 96%)
Gene name: MYCTH_40885
Sequence domains: GDSL-like Lipase/Acylhydrolase

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, BMA, MAN
Carbohydrate polymer
6 bound ligands:
Ligand B3P 1 x B3P
Ligand PEG 4 x PEG
Ligand ACT 3 x ACT
Ligand EDO 14 x EDO
Ligand NAG 1 x NAG
Ligand PG4 1 x PG4
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P3221
Unit cell:
a: 82.542Å b: 82.542Å c: 101.073Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.168 0.167 0.183
Expression system: Komagataella pastoris

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Citations

1 citations in other articles

Tryptophan production by catalysis of a putative tryptophan synthase protein.
Cao et al. (2024)

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